ID   RECF_ACIC1              Reviewed;         371 AA.
AC   A0LQR9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; OrderedLocusNames=Acel_0003;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC       required for DNA replication and normal SOS inducibility. RecF binds
CC       preferentially to single-stranded, linear DNA. It also seems to bind
CC       ATP. {ECO:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00365}.
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DR   EMBL; CP000481; ABK51779.1; -; Genomic_DNA.
DR   RefSeq; WP_011718843.1; NC_008578.1.
DR   AlphaFoldDB; A0LQR9; -.
DR   SMR; A0LQR9; -.
DR   STRING; 351607.Acel_0003; -.
DR   PRIDE; A0LQR9; -.
DR   EnsemblBacteria; ABK51779; ABK51779; Acel_0003.
DR   KEGG; ace:Acel_0003; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_1_1_11; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1050.90; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00365; RecF; 1.
DR   InterPro; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00611; recf; 1.
DR   PROSITE; PS00617; RECF_1; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..371
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000048498"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   371 AA;  41248 MW;  F333BE0B8DDD0BDE CRC64;
     MYLSRLELTD FRSYRRAALE LDPGVNVFVG SNGQGKTNLV EAVCYLALLR SHRTATDAPL
     VRQGSERAVL HGEVLTSGRR IDLDVEIVPG RANRLRVNGH ATRRARDLVG ILRVVIFAPE
     DLALVKGDPA ARRDYLDDVL VELRPRLFAV RAEYEKALRQ RNAFLRAVAQ DGQQVDRNSL
     DVWNLHFARA AAALLDARRR LVHELAPFVE KAYAAISGGS GAVRLEYRST VPEEVLQDAD
     EETRIAGILA ALRKVQDAEL ARGLTLVGPH RDDLNLELDS RPARGYASHG ESWSYALALR
     LGAYELLRSD GETPVMILDD VYAELDQQRR RRLTGCVSGA EQLLITSAVD EPDLPVGRRY
     VVHESQVHVA D